Related Experiment Video
Updated: Jun 29, 2026

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
Published on: July 1, 2021
Fluctuation analysis of mechanochemical coupling depending on the type of biomolecular motors
Masatoshi Nishikawa1, Hiroaki Takagi, Tatsuo Shibata
1Graduate School of Frontier Biosciences, Osaka University, Osaka, Japan. masnishi@hiroshima-u.ac.jp
Abstract:
Mechanochemical coupling was studied for myosin II and V consistently. The fluctuation in myosin V motility was determined by correlating the stochasticity of the ATPase reaction with regular displacements per one ATP, consistent with a tight mechanochemical coupling. In contrast, myosin II, working in an ensemble, was explained by a loose coupling, generating variable step sizes which depend on [ATP] and realizing a much larger step (200 nm) per one ATP than myosin V through its cooperativity at zero load. These different mechanics are ideal for their physiological functions.
Related Concept Videos
Mechanical Protein Functions
Anaphase A and B
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
The Movement of Organelles and Vesicles
Studying the Cytoskeleton
Actin Polymerization and Cell Motility
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
Microtubule Associated Motor Proteins

